ID A0A103XF97_CYNCS Unreviewed; 380 AA.
AC A0A103XF97;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=monodehydroascorbate reductase (NADH) {ECO:0000256|ARBA:ARBA00038920};
DE EC=1.6.5.4 {ECO:0000256|ARBA:ARBA00038920};
GN ORFNames=Ccrd_008347 {ECO:0000313|EMBL:KVH89660.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH89660.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH89660.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH89660.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
CC -!- FUNCTION: Catalyzes the conversion of monodehydroascorbate to
CC ascorbate, oxidizing NADH in the process.
CC {ECO:0000256|ARBA:ARBA00037189}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 monodehydro-L-ascorbate radical + NADH = 2 L-
CC ascorbate + NAD(+); Xref=Rhea:RHEA:14581, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:59513; EC=1.6.5.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036831};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00006442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVH89660.1}.
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DR EMBL; LEKV01005180; KVH89660.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XF97; -.
DR STRING; 59895.A0A103XF97; -.
DR EnsemblPlants; KVH89660; KVH89660; Ccrd_008347.
DR Gramene; KVH89660; KVH89660; Ccrd_008347.
DR OMA; RCTHYGA; -.
DR Proteomes; UP000243975; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR048618; MDHAR3-like_C.
DR PANTHER; PTHR43557; APOPTOSIS-INDUCING FACTOR 1; 1.
DR PANTHER; PTHR43557:SF5; MONODEHYDROASCORBATE REDUCTASE 1, PEROXISOMAL; 1.
DR Pfam; PF21791; MDHAR3-like_C; 1.
DR Pfam; PF07992; Pyr_redox_2; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975}.
FT DOMAIN 6..106
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 108..296
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 301..377
FT /note="Monodehydroascorbate reductase 3-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21791"
SQ SEQUENCE 380 AA; 40993 MW; 487C119FDE522D34 CRC64;
MAEKSFKYVI VGGGVSAGYA AREFAKQGVQ PGELAIISKE AVAPYERPAL SKAYLFPEGA
ARLPGFHVCV GSGGERLLPE WYTEKGISLI LNTEIVKADL ASKTLTNFGV QGADSKNIFY
LREIDNADKL VEIIKAKKTG TAIVVGGGYI GLELSAVLKI NNFDVKMVYP EPWCMPRLFT
ADIAAFYEAY YAKKGIDIIK GTVAVGFTSN DNGEVKEVKL KDGRVLEADI VVVGVGARPL
TNLFKGQVEE EKGGIKTDEF FKTSLPDVYA VGDVATFPMK MYGDIRRVEH VDHSRKSAEQ
AVKFYGDNVG DAVIFGDHDP ASAKPKFGSY WIKDGKVVGA FLEGGAPEEN QAIAKVAKLQ
PSASSLDVLA KEGLEFASKI
//
